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  • Catalase  (1)
  • Isonorastacene synthesis  (1)
  • 1
    ISSN: 0947-3440
    Keywords: Carotenoids ; Isonorastacene synthesis ; Singlet oxygen ; Effective chain length ; Second-order quenching rate constants ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The bimolecular rate constants kq for quenching of singlet oxygen (1Δg state) by 26 different natural and novel synthetic carotenoids were determined at 37 °C in a mixture of chloroform and ethanol. The steady-state technique used involves the generation of 1O2 by thermal decomposition of disodium 3,3′-naphtalene-1,4-diyl-dipropionate endoperoxide (NDPO2) and the detection of its luminescence intensity at 1270 nm. Excitation energies (π,π*, 11Ag → 11Bu) and absorption maxima (430-590 nm) vary in the broadest range. Deeply coloured blue carotenoids are also included in the studies for the first time. An empirical correlation between the π,π* (11Ag → 11Bu) excitation energy and carotenoid structure (effective chain length Neff) was found: E(S) = 12642 cm-1 + 92027 cm-1 × 1/Neff. The quenching ability of the investigated carotenoids depends on the excitation energy of their transition at long wavelengths in a characteristic way showing as limiting factors either the thermal Arrhenius activation or the diffusion-controlled rate. This dependence and the suspected relationship between singlet E(S) and triplet E(T) energies, respectively, are discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 13 (1974), S. 706-718 
    ISSN: 0570-0833
    Keywords: Catalase ; Peroxysomes ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The marker enzyme of the peroxisome - a phylogenetically old yet only recently discovered cell organelle - is catalase, a hemoprotein which decomposes hydrogen peroxide catalatically as well as peroxidatically. In the peroxisomes, catalase is associated with H2O2-producing oxidases and other enzymes. Also in parenchymal cells such as liver and kidney cells part of the reduction of oxygen occurs via formation of H2O2. A central role in peroxisomal H2O2-metabolism is played by the active intermediate, catalase-Fe3+-H2O2, (Compound I), which is distinguished from free catalase by specific absorption bands. Organ photometry on intact hemoglobin-free perfused rat liver in order to measure Compound I selectively provides a direct insight into the dynamics of the H2O2 metabolism which takes place in the range of nanomolar concentrations. Endogenously, 1g of liver forms approximately 50 nmol of H2O2 per min. The turnover number, which in the steady state is 〈 10 min-1 in the cell as compared to 〉 108 min-1 for the isolated enzyme with an excess of substrate, can be increased to approximately 102 min-1 by intracellular stimulation of the H2O2 production (e.g. by glycolate or urate). The peroxidatic oxidation of hydrogen donors (e.g. methanol and ethanol), favored relative to the catalase pathway at low turnover numbers, is of importance in normal metabolism and in pathological conditions.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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